[{"id":243044,"pmid":28732565,"pmcid":null,"title":"Circulating irisin levels are lower in patients with either stable coronary artery disease (CAD) or myocardial infarction (MI) versus healthy controls, whereas follistatin and activin A levels are higher and can discriminate MI from CAD with similar to CK-MB accuracy.","year":2017,"pages":null,"doi":null,"keywords":[],"mesh":[],"abstractText":"Several myokines are produced by cardiac muscle. We investigated changes in myokine levels at the time of acute myocardial infarction (MI) and following reperfusion in relation to controls.","journal":null,"figures":[],"_authors":null},{"id":403070,"pmid":28257634,"pmcid":null,"title":"Structural basis for potency differences between GDF8 and GDF11.","year":2017,"pages":null,"doi":null,"keywords":[],"mesh":[],"abstractText":"Growth/differentiation factor 8 (GDF8) and GDF11 are two highly similar members of the transforming growth factor ? (TGF?) family. While GDF8 has been recognized as a negative regulator of muscle growth and differentiation, there are conflicting studies on the function of GDF11 and whether GDF11 has beneficial effects on age-related dysfunction. To address whether GDF8 and GDF11 are functionally identical, we compared their signaling and structural properties.","journal":null,"figures":[],"_authors":null},{"id":529723,"pmid":27807065,"pmcid":null,"title":"Clinical and Therapeutic Implications of Follistatin in Solid Tumours.","year":null,"pages":null,"doi":null,"keywords":[],"mesh":[],"abstractText":"Follistatin (FST), as a single-chain glycosylated protein, has two major isoforms, FST288 and FST315. The FST315 isoform is the predominant form whilst the FST288 variant accounts for less than 5% of the encoded mRNA. FST is differentially expressed in human tissues and aberrant expression has been observed in a variety of solid tumours, including gonadal, gastric and lung cancer, hepatocellular carcinoma, basal cell carcinoma and melanoma. Based on the current evidence, FST is an antagonist of transforming growth factor beta family members, such as activin and bone morphogenetic proteins (BMPs). FST plays a role in tumourigenesis, metastasis and angiogenesis of solid tumours through its interaction with activin and BMPs, thus resulting in pathophysiological function. In terms of diagnosis, prognosis and therapy, FST has shown strong promise. Through a better understanding of its biological functions, potential clinical applications may yet emerge.","journal":null,"figures":[],"_authors":null},{"id":529722,"pmid":27787698,"pmcid":null,"title":"The transgenic expression of human follistatin-344 increases skeletal muscle mass in pigs.","year":2017,"pages":null,"doi":null,"keywords":[],"mesh":[],"abstractText":"Follistatin (FST), which was first found in the follicles of cattle and pigs, has been shown to be an essential regulator for muscle development. Mice that were genetically engineered to overexpress Fst specifically in muscle had at least twice the amount of skeletal muscle mass as controls; these findings are similar to earlier results obtained in myostatin-knockout mice. However, the role of follistatin in skeletal muscle development has yet to be clarified in livestock. Here, we describe transgenic Duroc pigs that exogenously express Fst specifically in muscle tissue. The transgenic pigs exhibited an increased proportion of skeletal muscle and a reduced proportion of body fat that were similar to those reported in myostatin-null cattle. The lean percentage of lean meat was significantly higher in the F1 generation of TG pigs (72.95 ± 1.0 %) than in WT pigs (69.18 ± 0.97 %) (N = 16, P